1knx | pdb_00001knx

HPr kinase/phosphatase from Mycoplasma pneumoniae

spinqualitylabelsall models 1knx, resolution 2.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1knx is a 6 chain structure with sequence from "filterable_agent_of_primary_atypical_pneumonia"_eaton_et_al._1944 "filterable agent of primary atypical pneumonia" eaton et al. 1944. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [HPRK_MYCPN] Is a metabolite-sensitive enzyme that catalyzes the ATP-as well as probably the pyrophosphate-dependent phosphorylation of Ser-47 in HPr, a phosphocarrier protein of the phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS). HprK/P also catalyzes the pyrophosphate-producing, inorganic phosphate-dependent dephosphorylation (phosphorolysis) of seryl-phosphorylated HPr (P-Ser-HPr). The regulatory role of HPrK/P in the physiology of M.pneumoniae is not known yet.[HAMAP-Rule:MF_01249] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed HPr kinase/phosphatase (HPrK/P) modifies serine 46 of histidine-containing protein (HPr), the phosphorylation state of which is the control point of carbon catabolite repression in low G+C Gram-positive bacteria. To understand the structural mechanism by which HPrK/P carries out its dual, competing activities we determined the structure of full length HPrK/P from Mycoplasma pneumoniae (PD8 ID, 1KNX) to 2.5A resolution. The enzyme forms a homo-hexamer with each subunit containing two domains connected by a short loop. The C-terminal domain contains the well-described P-loop (Walker A box) ATP binding motif and takes a fold similar to phosphoenolpyruvate carboxykinase (PEPCK) from Escherichia coli as recently described in other HPrK/P structures. As expected, the C-terminal domain is very similar to the C-terminal fragment of Lactobacillus casei HPrK/P and the C-terminal domain of Staphylococcus xylosus HPrK/P; the N-terminal domain is very similar to the N-terminal domain of S.xylosus HPrK/P. Unexpectedly, the N-terminal domain resembles UDP-N-acetylmuramoyl-L-alanyl-D-glutamate:meso-diaminopimelate ligase (MurE), yet the function of this domain is unclear. We discuss these observations as well as the structural significance of mutations in the P-loop and HPrK/P family sequence motif. Crystal structure of HPr kinase/phosphatase from Mycoplasma pneumoniae.,Allen GS, Steinhauer K, Hillen W, Stulke J, Brennan RG J Mol Biol. 2003 Feb 28;326(4):1203-17. PMID:12589763 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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